Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA.
Mov Disord. 2010;25 Suppl 1:S21-6. doi: 10.1002/mds.22722.
Despite considerable evidence linking alpha-synuclein with membranes in vitro, it has proven difficult to demonstrate membrane association of the protein in vivo. alpha-Synuclein localizes to the nerve terminal, but biochemical experiments have not revealed a tight association with membranes. To address the dynamics of the protein in live cells, we have used photobleaching and found that alpha-synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of alpha-synuclein, causing its dispersion from the synapse. In addition to the presumed role of alpha-synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease.
尽管有大量证据表明α-突触核蛋白与体外膜有关，但在体内证明该蛋白与膜的结合一直很困难。α-突触核蛋白定位于神经末梢，但生化实验并未揭示其与膜的紧密结合。为了研究活细胞中蛋白质的动力学，我们使用光漂白法发现α-突触核蛋白表现出高迁移率，尽管明显低于完全可溶性蛋白质。此外，神经活动控制α-突触核蛋白的分布，导致其从突触中分散。除了α-突触核蛋白动力学在突触功能中的假定作用外，其生理行为的变化可能是帕金森病相关病理变化的基础。
